DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Molecular basis for H3K36me3 recognition by the Tudor domain of PHF1. Molecular basis for H3K36me3 recognition by the Tudor domain of PHF1. Nature structural & molecular biology 2012 imex curation Musselman CA., Avvakumov N., Watanabe R., Abraham CG., Lalonde ME., Hong Z., Allen C., Roy S., Nuñez JK., Nickoloff J., Kulesza CA., Yasui A., Côté J., Kutateladze TG. Only protein-protein interactions mouse Mus musculus Mouse anti tag coip anti tag coimmunoprecipitation anti tag coip ms participant Identification by mass spectrometry ms participant Musselman CA., Avvakumov N., Watanabe R., Abraham CG., Lalonde ME., Hong Z., Allen C., Roy S., Nuñez JK., Nickoloff J., Kulesza CA., Yasui A., Côté J., Kutateladze TG. DIP original experiment: DIP-251439X Nature structural & molecular biology 2012 IMEx Molecular basis for H3K36me3 recognition by the Tudor domain of PHF1. Molecular basis for H3K36me3 recognition by the Tudor domain of PHF1. Molecular basis for H3K36me3 recognition by the Tudor domain of PHF1. Nature structural & molecular biology 2012 imex curation Musselman CA., Avvakumov N., Watanabe R., Abraham CG., Lalonde ME., Hong Z., Allen C., Roy S., Nuñez JK., Nickoloff J., Kulesza CA., Yasui A., Côté J., Kutateladze TG. Only protein-protein interactions in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Musselman CA., Avvakumov N., Watanabe R., Abraham CG., Lalonde ME., Hong Z., Allen C., Roy S., Nuñez JK., Nickoloff J., Kulesza CA., Yasui A., Côté J., Kutateladze TG. DIP original experiment: DIP-251429X Nature structural & molecular biology 2012 IMEx Molecular basis for H3K36me3 recognition by the Tudor domain of PHF1. Molecular basis for H3K36me3 recognition by the Tudor domain of PHF1. Molecular basis for H3K36me3 recognition by the Tudor domain of PHF1. Nature structural & molecular biology 2012 imex curation Musselman CA., Avvakumov N., Watanabe R., Abraham CG., Lalonde ME., Hong Z., Allen C., Roy S., Nuñez JK., Nickoloff J., Kulesza CA., Yasui A., Côté J., Kutateladze TG. Only protein-protein interactions in vitro In vitro pull down pull down predetermined predetermined participant predetermined Musselman CA., Avvakumov N., Watanabe R., Abraham CG., Lalonde ME., Hong Z., Allen C., Roy S., Nuñez JK., Nickoloff J., Kulesza CA., Yasui A., Côté J., Kutateladze TG. DIP original experiment: DIP-251430X Nature structural & molecular biology 2012 IMEx Molecular basis for H3K36me3 recognition by the Tudor domain of PHF1. Molecular basis for H3K36me3 recognition by the Tudor domain of PHF1. Molecular basis for H3K36me3 recognition by the Tudor domain of PHF1. Nature structural & molecular biology 2012 imex curation Musselman CA., Avvakumov N., Watanabe R., Abraham CG., Lalonde ME., Hong Z., Allen C., Roy S., Nuñez JK., Nickoloff J., Kulesza CA., Yasui A., Côté J., Kutateladze TG. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Musselman CA., Avvakumov N., Watanabe R., Abraham CG., Lalonde ME., Hong Z., Allen C., Roy S., Nuñez JK., Nickoloff J., Kulesza CA., Yasui A., Côté J., Kutateladze TG. DIP original experiment: DIP-251432X Nature structural & molecular biology 2012 IMEx Molecular basis for H3K36me3 recognition by the Tudor domain of PHF1. Molecular basis for H3K36me3 recognition by the Tudor domain of PHF1. Molecular basis for H3K36me3 recognition by the Tudor domain of PHF1. Nature structural & molecular biology 2012 imex curation Musselman CA., Avvakumov N., Watanabe R., Abraham CG., Lalonde ME., Hong Z., Allen C., Roy S., Nuñez JK., Nickoloff J., Kulesza CA., Yasui A., Côté J., Kutateladze TG. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Musselman CA., Avvakumov N., Watanabe R., Abraham CG., Lalonde ME., Hong Z., Allen C., Roy S., Nuñez JK., Nickoloff J., Kulesza CA., Yasui A., Côté J., Kutateladze TG. DIP original experiment: DIP-251436X Nature structural & molecular biology 2012 IMEx Molecular basis for H3K36me3 recognition by the Tudor domain of PHF1. Molecular basis for H3K36me3 recognition by the Tudor domain of PHF1. Molecular basis for H3K36me3 recognition by the Tudor domain of PHF1. Nature structural & molecular biology 2012 imex curation Musselman CA., Avvakumov N., Watanabe R., Abraham CG., Lalonde ME., Hong Z., Allen C., Roy S., Nuñez JK., Nickoloff J., Kulesza CA., Yasui A., Côté J., Kutateladze TG. Only protein-protein interactions human Homo sapiens Human anti tag coip anti tag coimmunoprecipitation anti tag coip western blot western blot Immuno blot Immuno blot Musselman CA., Avvakumov N., Watanabe R., Abraham CG., Lalonde ME., Hong Z., Allen C., Roy S., Nuñez JK., Nickoloff J., Kulesza CA., Yasui A., Côté J., Kutateladze TG. DIP original experiment: DIP-251428X Nature structural & molecular biology 2012 IMEx Molecular basis for H3K36me3 recognition by the Tudor domain of PHF1. Molecular basis for H3K36me3 recognition by the Tudor domain of PHF1. Molecular basis for H3K36me3 recognition by the Tudor domain of PHF1. Nature structural & molecular biology 2012 imex curation Musselman CA., Avvakumov N., Watanabe R., Abraham CG., Lalonde ME., Hong Z., Allen C., Roy S., Nuñez JK., Nickoloff J., Kulesza CA., Yasui A., Côté J., Kutateladze TG. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Musselman CA., Avvakumov N., Watanabe R., Abraham CG., Lalonde ME., Hong Z., Allen C., Roy S., Nuñez JK., Nickoloff J., Kulesza CA., Yasui A., Côté J., Kutateladze TG. DIP original experiment: DIP-251437X Nature structural & molecular biology 2012 IMEx Molecular basis for H3K36me3 recognition by the Tudor domain of PHF1. Molecular basis for H3K36me3 recognition by the Tudor domain of PHF1. Molecular basis for H3K36me3 recognition by the Tudor domain of PHF1. Nature structural & molecular biology 2012 imex curation Musselman CA., Avvakumov N., Watanabe R., Abraham CG., Lalonde ME., Hong Z., Allen C., Roy S., Nuñez JK., Nickoloff J., Kulesza CA., Yasui A., Côté J., Kutateladze TG. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Musselman CA., Avvakumov N., Watanabe R., Abraham CG., Lalonde ME., Hong Z., Allen C., Roy S., Nuñez JK., Nickoloff J., Kulesza CA., Yasui A., Côté J., Kutateladze TG. DIP original experiment: DIP-251438X Nature structural & molecular biology 2012 IMEx Molecular basis for H3K36me3 recognition by the Tudor domain of PHF1. Molecular basis for H3K36me3 recognition by the Tudor domain of PHF1. Molecular basis for H3K36me3 recognition by the Tudor domain of PHF1. Nature structural & molecular biology 2012 imex curation Musselman CA., Avvakumov N., Watanabe R., Abraham CG., Lalonde ME., Hong Z., Allen C., Roy S., Nuñez JK., Nickoloff J., Kulesza CA., Yasui A., Côté J., Kutateladze TG. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Musselman CA., Avvakumov N., Watanabe R., Abraham CG., Lalonde ME., Hong Z., Allen C., Roy S., Nuñez JK., Nickoloff J., Kulesza CA., Yasui A., Côté J., Kutateladze TG. DIP original experiment: DIP-251435X Nature structural & molecular biology 2012 IMEx Molecular basis for H3K36me3 recognition by the Tudor domain of PHF1. Molecular basis for H3K36me3 recognition by the Tudor domain of PHF1. Molecular basis for H3K36me3 recognition by the Tudor domain of PHF1. Nature structural & molecular biology 2012 imex curation Musselman CA., Avvakumov N., Watanabe R., Abraham CG., Lalonde ME., Hong Z., Allen C., Roy S., Nuñez JK., Nickoloff J., Kulesza CA., Yasui A., Côté J., Kutateladze TG. Only protein-protein interactions in vitro In vitro pull down pull down predetermined predetermined participant predetermined Musselman CA., Avvakumov N., Watanabe R., Abraham CG., Lalonde ME., Hong Z., Allen C., Roy S., Nuñez JK., Nickoloff J., Kulesza CA., Yasui A., Côté J., Kutateladze TG. DIP original experiment: DIP-251431X Nature structural & molecular biology 2012 IMEx Molecular basis for H3K36me3 recognition by the Tudor domain of PHF1. Molecular basis for H3K36me3 recognition by the Tudor domain of PHF1. Molecular basis for H3K36me3 recognition by the Tudor domain of PHF1. Nature structural & molecular biology 2012 imex curation Musselman CA., Avvakumov N., Watanabe R., Abraham CG., Lalonde ME., Hong Z., Allen C., Roy S., Nuñez JK., Nickoloff J., Kulesza CA., Yasui A., Côté J., Kutateladze TG. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Musselman CA., Avvakumov N., Watanabe R., Abraham CG., Lalonde ME., Hong Z., Allen C., Roy S., Nuñez JK., Nickoloff J., Kulesza CA., Yasui A., Côté J., Kutateladze TG. DIP original experiment: DIP-251433X Nature structural & molecular biology 2012 IMEx Molecular basis for H3K36me3 recognition by the Tudor domain of PHF1. Molecular basis for H3K36me3 recognition by the Tudor domain of PHF1. Molecular basis for H3K36me3 recognition by the Tudor domain of PHF1. Nature structural & molecular biology 2012 imex curation Musselman CA., Avvakumov N., Watanabe R., Abraham CG., Lalonde ME., Hong Z., Allen C., Roy S., Nuñez JK., Nickoloff J., Kulesza CA., Yasui A., Côté J., Kutateladze TG. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Musselman CA., Avvakumov N., Watanabe R., Abraham CG., Lalonde ME., Hong Z., Allen C., Roy S., Nuñez JK., Nickoloff J., Kulesza CA., Yasui A., Côté J., Kutateladze TG. DIP original experiment: DIP-251434X Nature structural & molecular biology 2012 IMEx Molecular basis for H3K36me3 recognition by the Tudor domain of PHF1. h3k9-2 Histone H3 N-terminal Peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) ARTKQTARKSTGGKAPRKQLA phf1_human PHD finger protein 1 PCL1 Polycomb-like protein 1 PHF1 protein protein human Homo sapiens Human MAQPPRLSRSGASSLWDPASPAPTSGPRPRLWEGQDVLARWTDGLLYLGTIKKVDSAREVCLVQFEDDSQFLVLWKDISPAALPGEELLCCVCRSETVVPGNRLVSCEKCRHAYHQDCHVPRAPAPGEGEGTSWVCRQCVFAIATKRGGALKKGPYARAMLGMKLSLPYGLKGLDWDAGHLSNRQQSYCYCGGPGEWNLKMLQCRSCLQWFHEACTQCLSKPLLYGDRFYEFECCVCRGGPEKVRRLQLRWVDVAHLVLYHLSVCCKKKYFDFDREILPFTSENWDSLLLGELSDTPKGERSSRLLSALNSHKDRFISGREIKKRKCLFGLHARMPPPVEPPTGDGALTSFPSGQGPGGGVSRPLGKRRRPEPEPLRRRQKGKVEELGPPSAVRNQPEPQEQRERAHLQRALQASVSPPSPSPNQSYQGSSGYNFRPTDARCLPSSPIRMFASFHPSASTAGTSGDSGPPDRSPLELHIGFPTDIPKSAPHSMTASSSSVSSPSPGLPRRSAPPSPLCRSLSPGTGGGVRGGVGYLSRGDPVRVLARRVRPDGSVQYLVEWGGGGIF DIP protein O43189 original sequence version: 124 E81BA9475565957C rbbp4_mouse Histone-binding protein RBBP4 Rbbp4 Rbap48 Retinoblastoma-binding protein 4 Retinoblastoma-binding protein p48 Chromatin assembly factor 1 subunit C Chromatin assembly factor I p48 subunit Nucleosome-remodeling factor subunit RBAP48 protein protein mouse Mus musculus Mouse MADKEAAFDDAVEERVINEEYKIWKKNTPFLYDLVMTHALEWPSLTAQWLPDVTRPEGKDFSIHRLVLGTHTSDEQNHLVIASVQLPNDDAQFDASHYDSEKGEFGGFGSVSGKIEIEIKINHEGEVNRARYMPQNPCIIATKTPSSDVLVFDYTKHPSKPDPSGECNPDLRLRGHQKEGYGLSWNPNLSGHLLSASDDHTICLWDISAVPKEGKVVDAKTIFTGHTAVVEDVSWHLLHESLFGSVADDQKLMIWDTRSNNTSKPSHSVDAHTAEVNCLSFNPYSEFILATGSADKTVALWDLRNLKLKLHSFESHKDEIFQVQWSPHNETILASSGTDRRLNVWDLSKIGEEQSPEDAEDGPPELLFIHGGHTAKISDFSWNPNEPWVICSVSEDNIMQVWQMAENIYNDEDPEGSVDPEGQGS DIP protein Q60972 original sequence version: 141 DIP protein Q60972 original sequence version: 117 DIP protein Q60972 original sequence version: 115 B71E2D55A444C360 h3k27me Histone 3 fragment [ATKAARKSAPATGGVKKPHRYRPG] peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) ATKAARKSAPATGGVKKPHRYRPG suz12_mouse Polycomb protein Suz12 Suz12 D11Ertd530e Kiaa0160 Suppressor of zeste 12 protein homolog protein protein mouse Mus musculus Mouse MAPQKHGGGGGGGSGPSAGSGGGGFGGSAAAVAAAASGGKSGGGGCGGGGSYSASSSSAAAAAAAAGAAVLPVKKPKMEHVQADHELFLQAFEKPTQIYRFLRTRNLIAPIFLHRTLTYMSHRNSRTSIKRKTFKVDDMLSKVEKMKGEQESHSLSAHLQLTFTGFFHKNDKPSQNSENEQNSVTLEVLLVKVCHKKRKDVSCPIRQVPTGKKQVPLNPDLNQTKPGNFPSLAVSSNEFEPSNSHMVKSYSLLFRVTRPGRREFNGMINGETNENIDVSEELPARRKRNREDGEKTFVAQMTVFDKNRRLQLLDGEYEVAMQEMEECPISKKRATWETILDGKRLPPFETFSQGPTLQFTLRWTGETNDKSTAPVAKPLATRNSESLHQENKPGSVKPAQTIAVKETLTTELQTRKEKDNSNESRQKLRIFYQFLYNNNTRQQTEARDDLHCPWCTLNCRKLYSLLKHLKLCHSRFIFNYVYHPKGARIDVSINECYDGSYAGNPQDIHRQPGFAFSRNGPVKRTPITHILVCRPKRTKASMSEFLESEDGEVEQQRTYSSGHNRLYFHSDTCLPLRPQEMEVDSEDEKDPEWLREKTITQIEEFSDVNEGEKEVMKLWNLHVMKHGFIADNQMNHACMLFVENYGQKIIKKNLCRNFMLHLVSMHDFNLISIMSIDKAVTKLREMQQKLEKGESATPSNEEIAEEQNGTANGFSETNSKEKALETDGVSGVPKQSKKQKL DIP protein Q80U70 original sequence version: 62 DIP protein Q80U70 original sequence version: 85 DIP protein Q80U70 original sequence version: 84 4A6B6E52D24FAEF2 eed_mouse Polycomb protein EED Eed protein protein mouse Mus musculus Mouse MSEREVSTAPAGTDMPAAKKQKLSSDENSNPDLSGDENDDAVSIESGTNTERPDTPTNTPNAPGRKSWGKGKWKSKKCKYSFKCVNSLKEDHNQPLFGVQFNWHSKEGDPLVFATVGSNRVTLYECHSQGEIRLLQSYVDADADENFYTCAWTYDSNTSHPLLAVAGSRGIIRIINPITMQCIKHYVGHGNAINELKFHPRDPNLLLSVSKDHALRLWNIQTDTLVAIFGGVEGHRDEVLSADYDLLGEKIMSCGMDHSLKLWRINSKRMMNAIKESYDYNPNKTNRPFISQKIHFPDFSTRDIHRNYVDCVRWLGDLILSKSCENAIVCWKPGKMEDDIDKIKPSESNVTILGRFDYSQCDIWYMRFSMDFWQKMLALGNQVGKLYVWDLEVEDPHKAKCTTLTHHKCGAAIRQTSFSRDSSILIAVCDDASIWRWDRLR DIP protein Q921E6 original sequence version: 48 DIP protein Q921E6 original sequence version: 73 DIP protein Q921E6 original sequence version: 98 D2E0A5BA27C0499A q61188-1 Histone-lysine N-methyltransferase EZH2 Ezh2 Enx1h ENX-1 Enhancer of zeste homolog 2 protein protein mouse Mus musculus Mouse MGQTGKKSEKGPVCWRKRVKSEYMRLRQLKRFRRADEVKTMFSSNRQKILERTETLNQEWKQRRIQPVHIMTSVSSLRGTRECSVTSDLDFPAQVIPLKTLNAVASVPIMYSWSPLQQNFMVEDETVLHNIPYMGDEVLDQDGTFIEELIKNYDGKVHGDRECGFINDEIFVELVNALGQYNDDDDDDDGDDPDEREEKQKDLEDNRDDKETCPPRKFPADKIFEAISSMFPDKGTAEELKEKYKELTEQQLPGALPPECTPNIDGPNAKSVQREQSLHSFHTLFCRRCFKYDCFLHPFHATPNTYKRKNTETALDNKPCGPQCYQHLEGAKEFAAALTAERIKTPPKRPGGRRRGRLPNNSSRPSTPTISVLESKDTDSDREAGTETGGENNDKEEEEKKDETSSSSEANSRCQTPIKMKPNIEPPENVEWSGAEASMFRVLIGTYYDNFCAIARLIGTKTCRQVYEFRVKESSIIAPVPTEDVDTPPRKKKRKHRLWAAHCRKIQLKKDGSSNHVYNYQPCDHPRQPCDSSCPCVIAQNFCEKFCQCSSECQNRFPGCRCKAQCNTKQCPCYLAVRECDPDLCLTCGAADHWDSKNVSCKNCSIQRGSKKHLLLAPSDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVYDKYMCSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKVMMVNGDHRIGIFAKRAIQTGEELFFDYRYSQADALKYVGIEREMEIP DIP protein Q61188-1 original sequence version: 64 DIP protein Q61188 original sequence version: 87 DIP protein Q61188 original sequence version: 114 DIP protein Q61188 original sequence version: 108 ezh2_human Histone-lysine N-methyltransferase EZH2 KMT6 Enhancer of zeste homolog 2 ENX-1 Lysine N-methyltransferase 6 EZH2 protein protein human Homo sapiens Human MGQTGKKSEKGPVCWRKRVKSEYMRLRQLKRFRRADEVKSMFSSNRQKILERTEILNQEWKQRRIQPVHILTSVSSLRGTRECSVTSDLDFPTQVIPLKTLNAVASVPIMYSWSPLQQNFMVEDETVLHNIPYMGDEVLDQDGTFIEELIKNYDGKVHGDRECGFINDEIFVELVNALGQYNDDDDDDDGDDPEEREEKQKDLEDHRDDKESRPPRKFPSDKIFEAISSMFPDKGTAEELKEKYKELTEQQLPGALPPECTPNIDGPNAKSVQREQSLHSFHTLFCRRCFKYDCFLHPFHATPNTYKRKNTETALDNKPCGPQCYQHLEGAKEFAAALTAERIKTPPKRPGGRRRGRLPNNSSRPSTPTINVLESKDTDSDREAGTETGGENNDKEEEEKKDETSSSSEANSRCQTPIKMKPNIEPPENVEWSGAEASMFRVLIGTYYDNFCAIARLIGTKTCRQVYEFRVKESSIIAPAPAEDVDTPPRKKKRKHRLWAAHCRKIQLKKDGSSNHVYNYQPCDHPRQPCDSSCPCVIAQNFCEKFCQCSSECQNRFPGCRCKAQCNTKQCPCYLAVRECDPDLCLTCGAADHWDSKNVSCKNCSIQRGSKKHLLLAPSDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVYDKYMCSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKVMMVNGDHRIGIFAKRAIQTGEELFFDYRYSQADALKYVGIEREMEIP DIP protein Q15910 original sequence version: 97 DIP protein Q15910 original sequence version: 94 DIP protein Q15910 original sequence version: 92 DIP protein Q15910 original sequence version: 96 DIP protein Q15910 original sequence version: 122 DIP protein Q15910 original sequence version: 100 1B5029EB9D509BE5 h4(1523) Histone 4 peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) AKRHRKVLR h3(2240) Histone 3 peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) TKAARKSAPSTGGVKKPHR h3(121)-phf1-1 3 13 unspecified role unspecified role bait bait K4me2 K4me2 n6me2lys N6,N6-dimethyl-L-lysine (2S)-2-amino-6-(dimethylamino)hexanoic acid MOD_RES N6,N6-dimethyllysine N(zeta)-dimethyllysine N6,N6-dimethyl-L-lysine N6,N6-dimethylated L-lysine epsilon-dimethyllysine lysine derivative Lys(y) Dimethyl N6Me2Lys di-Methylation dimethylk certain certain sequence position certain certain certain sequence position certain K4me3 K4me3 n6me3+lys N6,N6,N6-trimethyl-L-lysine (5S)-5-amino-5-carboxy-N,N,N-trimethylpentan-1-aminium 2-amino-6-(trimethylammonio)hexanoic acid 5-azanyl-5-carboxy-N,N,N-trimethylpentanazanium MOD_RES N6,N6,N6-trimethyllysine N(zeta)-trimethyllysine N6,N6,N6-trimethyl-L-lysine N6,N6,N6-trimethylated L-lysine N6,N6,N6-trimethyllysin-N6-ium N6,N6,N6-trimethyllysine cation epsilon-trimethyllysine N-trimethylation (of lysine) N6Me3+Lys Trimethyl tri-Methylation certain certain sequence position certain certain certain sequence position certain K9me1 K9me1 n6me1lys N6-methyl-L-lysine (2S)-2-amino-6-methylaminohexanoic acid MOD_RES N6-methyllysine N(zeta)-methyllysine N6-methyl-L-lysine N6-methylated L-lysine epsilon-methyllysine Methyl Methylation N-methyl Lysyl N6Me1Lys certain certain sequence position certain certain certain sequence position certain K9me2 K9me2 n6me2lys N6,N6-dimethyl-L-lysine (2S)-2-amino-6-(dimethylamino)hexanoic acid MOD_RES N6,N6-dimethyllysine N(zeta)-dimethyllysine N6,N6-dimethyl-L-lysine N6,N6-dimethylated L-lysine epsilon-dimethyllysine lysine derivative Lys(y) Dimethyl N6Me2Lys di-Methylation dimethylk certain certain sequence position certain certain certain sequence position certain Biotin-tag Biotin-tag biotin tag biotin tag c-terminal c-terminal position c-term carboxy-terminus c-terminus c-term c-terminus carboxy-terminus c-terminal c-terminal c-terminal position c-term carboxy-terminus c-terminus c-term c-terminus carboxy-terminus c-terminal in vitro In vitro 14 unspecified role unspecified role prey prey Region 14-87 Region 14-87 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain GST-tag GST-tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli direct interaction direct interaction h3(2240)-phf1-1 8 22 unspecified role unspecified role unspecified role unspecified role K16me3 K16me3 n6me3+lys N6,N6,N6-trimethyl-L-lysine (5S)-5-amino-5-carboxy-N,N,N-trimethylpentan-1-aminium 2-amino-6-(trimethylammonio)hexanoic acid 5-azanyl-5-carboxy-N,N,N-trimethylpentanazanium MOD_RES N6,N6,N6-trimethyllysine N(zeta)-trimethyllysine N6,N6,N6-trimethyl-L-lysine N6,N6,N6-trimethylated L-lysine N6,N6,N6-trimethyllysin-N6-ium N6,N6,N6-trimethyllysine cation epsilon-trimethyllysine N-trimethylation (of lysine) N6Me3+Lys Trimethyl tri-Methylation certain certain sequence position certain certain certain sequence position certain Region 10-19 Region 10-19 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 14 unspecified role unspecified role unspecified role unspecified role Region 14-87 Region 14-87 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain O43189:p.Trp41Ala W41A mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain W A This feature has been corrected as a result of our quality control procedures. The original label was 'W41A'. Wed May 02 14:57:57 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'trp41ala' Tue Jun 30 18:48:56 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Trp41Ala' O43189:p.Tyr47Ala Y47A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain Y A This feature has been corrected as a result of our quality control procedures. The original label was 'Y47A'. Wed May 02 15:24:04 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr47ala' Tue Jun 30 16:28:37 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr47Ala' ecolx Escherichia coli direct interaction direct interaction phf1-ezh2-1 6 20 unspecified role unspecified role prey prey human Homo sapiens Human 14 unspecified role unspecified role bait bait Flag-tag Flag-tag flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged n-term range n-terminal range n-term range n-term range n-terminal range n-term range human Homo sapiens Human physical association physical association h3(2240)-phf1-2 9 22 unspecified role unspecified role unspecified role unspecified role Region 1-12 Region 1-12 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain K6me3 K6me3 n6me3+lys N6,N6,N6-trimethyl-L-lysine (5S)-5-amino-5-carboxy-N,N,N-trimethylpentan-1-aminium 2-amino-6-(trimethylammonio)hexanoic acid 5-azanyl-5-carboxy-N,N,N-trimethylpentanazanium MOD_RES N6,N6,N6-trimethyllysine N(zeta)-trimethyllysine N6,N6,N6-trimethyl-L-lysine N6,N6,N6-trimethylated L-lysine N6,N6,N6-trimethyllysin-N6-ium N6,N6,N6-trimethyllysine cation epsilon-trimethyllysine N-trimethylation (of lysine) N6Me3+Lys Trimethyl tri-Methylation certain certain sequence position certain certain certain sequence position certain in vitro In vitro 14 unspecified role unspecified role unspecified role unspecified role Region 14-87 Region 14-87 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction h3(2240)-phf1-3 5 22 unspecified role unspecified role unspecified role unspecified role Region 10-19 Region 10-19 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain K16me2 K16me2 n6me2lys N6,N6-dimethyl-L-lysine (2S)-2-amino-6-(dimethylamino)hexanoic acid MOD_RES N6,N6-dimethyllysine N(zeta)-dimethyllysine N6,N6-dimethyl-L-lysine N6,N6-dimethylated L-lysine epsilon-dimethyllysine lysine derivative Lys(y) Dimethyl N6Me2Lys di-Methylation dimethylk certain certain sequence position certain certain certain sequence position certain K16me3 K16me3 n6me3+lys N6,N6,N6-trimethyl-L-lysine (5S)-5-amino-5-carboxy-N,N,N-trimethylpentan-1-aminium 2-amino-6-(trimethylammonio)hexanoic acid 5-azanyl-5-carboxy-N,N,N-trimethylpentanazanium MOD_RES N6,N6,N6-trimethyllysine N(zeta)-trimethyllysine N6,N6,N6-trimethyl-L-lysine N6,N6,N6-trimethylated L-lysine N6,N6,N6-trimethyllysin-N6-ium N6,N6,N6-trimethyllysine cation epsilon-trimethyllysine N-trimethylation (of lysine) N6Me3+Lys Trimethyl tri-Methylation certain certain sequence position certain certain certain sequence position certain K16me1 K16me1 n6me1lys N6-methyl-L-lysine (2S)-2-amino-6-methylaminohexanoic acid MOD_RES N6-methyllysine N(zeta)-methyllysine N6-methyl-L-lysine N6-methylated L-lysine epsilon-methyllysine Methyl Methylation N-methyl Lysyl N6Me1Lys certain certain sequence position certain certain certain sequence position certain disrupting-ptm ptm disrupting an interaction disrupting-ptm in vitro In vitro 14 unspecified role unspecified role unspecified role unspecified role Region 14-87 Region 14-87 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction phf1-eed-1 1 15 unspecified role unspecified role prey prey mouse Mus musculus Mouse 18 unspecified role unspecified role prey prey mouse Mus musculus Mouse 17 unspecified role unspecified role prey prey mouse Mus musculus Mouse 19 unspecified role unspecified role prey prey mouse Mus musculus Mouse 14 unspecified role unspecified role bait bait Flag-tag Flag-tag flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged n-term range n-terminal range n-term range n-term range n-terminal range n-term range mouse Mus musculus Mouse association association h3(121)-phf1-2 11 13 unspecified role unspecified role unspecified role unspecified role K4me3 K4me3 n6me3+lys N6,N6,N6-trimethyl-L-lysine (5S)-5-amino-5-carboxy-N,N,N-trimethylpentan-1-aminium 2-amino-6-(trimethylammonio)hexanoic acid 5-azanyl-5-carboxy-N,N,N-trimethylpentanazanium MOD_RES N6,N6,N6-trimethyllysine N(zeta)-trimethyllysine N6,N6,N6-trimethyl-L-lysine N6,N6,N6-trimethylated L-lysine N6,N6,N6-trimethyllysin-N6-ium N6,N6,N6-trimethyllysine cation epsilon-trimethyllysine N-trimethylation (of lysine) N6Me3+Lys Trimethyl tri-Methylation certain certain sequence position certain certain certain sequence position certain Region 1-12 Region 1-12 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain K9me3 K9me3 n6me3+lys N6,N6,N6-trimethyl-L-lysine (5S)-5-amino-5-carboxy-N,N,N-trimethylpentan-1-aminium 2-amino-6-(trimethylammonio)hexanoic acid 5-azanyl-5-carboxy-N,N,N-trimethylpentanazanium MOD_RES N6,N6,N6-trimethyllysine N(zeta)-trimethyllysine N6,N6,N6-trimethyl-L-lysine N6,N6,N6-trimethylated L-lysine N6,N6,N6-trimethyllysin-N6-ium N6,N6,N6-trimethyllysine cation epsilon-trimethyllysine N-trimethylation (of lysine) N6Me3+Lys Trimethyl tri-Methylation certain certain sequence position certain certain certain sequence position certain in vitro In vitro 14 unspecified role unspecified role unspecified role unspecified role Region 14-87 Region 14-87 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction h3(2240)-phf1-4 2 22 unspecified role unspecified role unspecified role unspecified role Region 10-19 Region 10-19 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain K15me3 K15me3 n6me3+lys N6,N6,N6-trimethyl-L-lysine (5S)-5-amino-5-carboxy-N,N,N-trimethylpentan-1-aminium 2-amino-6-(trimethylammonio)hexanoic acid 5-azanyl-5-carboxy-N,N,N-trimethylpentanazanium MOD_RES N6,N6,N6-trimethyllysine N(zeta)-trimethyllysine N6,N6,N6-trimethyl-L-lysine N6,N6,N6-trimethylated L-lysine N6,N6,N6-trimethyllysin-N6-ium N6,N6,N6-trimethyllysine cation epsilon-trimethyllysine N-trimethylation (of lysine) N6Me3+Lys Trimethyl tri-Methylation certain certain sequence position certain certain certain sequence position certain in vitro In vitro 14 unspecified role unspecified role unspecified role unspecified role Region 28-87 Region 28-87 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction h3(2240)-phf1-5 12 22 unspecified role unspecified role unspecified role unspecified role Region 1-12 Region 1-12 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain K6me3 K6me3 n6me3+lys N6,N6,N6-trimethyl-L-lysine (5S)-5-amino-5-carboxy-N,N,N-trimethylpentan-1-aminium 2-amino-6-(trimethylammonio)hexanoic acid 5-azanyl-5-carboxy-N,N,N-trimethylpentanazanium MOD_RES N6,N6,N6-trimethyllysine N(zeta)-trimethyllysine N6,N6,N6-trimethyl-L-lysine N6,N6,N6-trimethylated L-lysine N6,N6,N6-trimethyllysin-N6-ium N6,N6,N6-trimethyllysine cation epsilon-trimethyllysine N-trimethylation (of lysine) N6Me3+Lys Trimethyl tri-Methylation certain certain sequence position certain certain certain sequence position certain in vitro In vitro 14 unspecified role unspecified role unspecified role unspecified role Region 14-87 Region 14-87 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction h4(1523)-phf1-1 4 21 unspecified role unspecified role unspecified role unspecified role K6me3 K6me3 n6me3+lys N6,N6,N6-trimethyl-L-lysine (5S)-5-amino-5-carboxy-N,N,N-trimethylpentan-1-aminium 2-amino-6-(trimethylammonio)hexanoic acid 5-azanyl-5-carboxy-N,N,N-trimethylpentanazanium MOD_RES N6,N6,N6-trimethyllysine N(zeta)-trimethyllysine N6,N6,N6-trimethyl-L-lysine N6,N6,N6-trimethylated L-lysine N6,N6,N6-trimethyllysin-N6-ium N6,N6,N6-trimethyllysine cation epsilon-trimethyllysine N-trimethylation (of lysine) N6Me3+Lys Trimethyl tri-Methylation certain certain sequence position certain certain certain sequence position certain in vitro In vitro 14 unspecified role unspecified role unspecified role unspecified role Region 14-87 Region 14-87 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction h3(2240)-phf1-6 7 22 unspecified role unspecified role unspecified role unspecified role Region 10-19 Region 10-19 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain K16me2 K16me2 n6me2lys N6,N6-dimethyl-L-lysine (2S)-2-amino-6-(dimethylamino)hexanoic acid MOD_RES N6,N6-dimethyllysine N(zeta)-dimethyllysine N6,N6-dimethyl-L-lysine N6,N6-dimethylated L-lysine epsilon-dimethyllysine lysine derivative Lys(y) Dimethyl N6Me2Lys di-Methylation dimethylk certain certain sequence position certain certain certain sequence position certain increasing-ptm ptm increasing an interaction increasing-ptm K16me3 K16me3 n6me3+lys N6,N6,N6-trimethyl-L-lysine (5S)-5-amino-5-carboxy-N,N,N-trimethylpentan-1-aminium 2-amino-6-(trimethylammonio)hexanoic acid 5-azanyl-5-carboxy-N,N,N-trimethylpentanazanium MOD_RES N6,N6,N6-trimethyllysine N(zeta)-trimethyllysine N6,N6,N6-trimethyl-L-lysine N6,N6,N6-trimethylated L-lysine N6,N6,N6-trimethyllysin-N6-ium N6,N6,N6-trimethyllysine cation epsilon-trimethyllysine N-trimethylation (of lysine) N6Me3+Lys Trimethyl tri-Methylation certain certain sequence position certain certain certain sequence position certain increasing-ptm ptm increasing an interaction increasing-ptm K16me1 K16me1 n6me1lys N6-methyl-L-lysine (2S)-2-amino-6-methylaminohexanoic acid MOD_RES N6-methyllysine N(zeta)-methyllysine N6-methyl-L-lysine N6-methylated L-lysine epsilon-methyllysine Methyl Methylation N-methyl Lysyl N6Me1Lys certain certain sequence position certain certain certain sequence position certain in vitro In vitro 14 unspecified role unspecified role unspecified role unspecified role Region 14-87 Region 14-87 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction h3(2144)-phf1-1 10 16 unspecified role unspecified role bait bait Biotin-tag Biotin-tag biotin tag biotin tag c-terminal c-terminal position c-term carboxy-terminus c-terminus c-term c-terminus carboxy-terminus c-terminal c-terminal c-terminal position c-term carboxy-terminus c-terminus c-term c-terminus carboxy-terminus c-terminal K7me2 K7me2 n6me2lys N6,N6-dimethyl-L-lysine (2S)-2-amino-6-(dimethylamino)hexanoic acid MOD_RES N6,N6-dimethyllysine N(zeta)-dimethyllysine N6,N6-dimethyl-L-lysine N6,N6-dimethylated L-lysine epsilon-dimethyllysine lysine derivative Lys(y) Dimethyl N6Me2Lys di-Methylation dimethylk certain certain sequence position certain certain certain sequence position certain K7me3 K7me3 n6me3+lys N6,N6,N6-trimethyl-L-lysine (5S)-5-amino-5-carboxy-N,N,N-trimethylpentan-1-aminium 2-amino-6-(trimethylammonio)hexanoic acid 5-azanyl-5-carboxy-N,N,N-trimethylpentanazanium MOD_RES N6,N6,N6-trimethyllysine N(zeta)-trimethyllysine N6,N6,N6-trimethyl-L-lysine N6,N6,N6-trimethylated L-lysine N6,N6,N6-trimethyllysin-N6-ium N6,N6,N6-trimethyllysine cation epsilon-trimethyllysine N-trimethylation (of lysine) N6Me3+Lys Trimethyl tri-Methylation certain certain sequence position certain certain certain sequence position certain K16me1 K16me1 n6me1lys N6-methyl-L-lysine (2S)-2-amino-6-methylaminohexanoic acid MOD_RES N6-methyllysine N(zeta)-methyllysine N6-methyl-L-lysine N6-methylated L-lysine epsilon-methyllysine Methyl Methylation N-methyl Lysyl N6Me1Lys certain certain sequence position certain certain certain sequence position certain K16me2 K16me2 n6me2lys N6,N6-dimethyl-L-lysine (2S)-2-amino-6-(dimethylamino)hexanoic acid MOD_RES N6,N6-dimethyllysine N(zeta)-dimethyllysine N6,N6-dimethyl-L-lysine N6,N6-dimethylated L-lysine epsilon-dimethyllysine lysine derivative Lys(y) Dimethyl N6Me2Lys di-Methylation dimethylk certain certain sequence position certain certain certain sequence position certain K16me3 K16me3 n6me3+lys N6,N6,N6-trimethyl-L-lysine (5S)-5-amino-5-carboxy-N,N,N-trimethylpentan-1-aminium 2-amino-6-(trimethylammonio)hexanoic acid 5-azanyl-5-carboxy-N,N,N-trimethylpentanazanium MOD_RES N6,N6,N6-trimethyllysine N(zeta)-trimethyllysine N6,N6,N6-trimethyl-L-lysine N6,N6,N6-trimethylated L-lysine N6,N6,N6-trimethyllysin-N6-ium N6,N6,N6-trimethyllysine cation epsilon-trimethyllysine N-trimethylation (of lysine) N6Me3+Lys Trimethyl tri-Methylation certain certain sequence position certain certain certain sequence position certain in vitro In vitro 14 unspecified role unspecified role prey prey Region 14-87 Region 14-87 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain GST-tag GST-tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli direct interaction direct interaction